Results 201 to 210 of about 95,153 (249)
Untargeted peptide profiling investigates how S. thermophilus, Lb. bulgaricus, and endogenous milk enzymes impact proteolysis during early‐stage milk fermentation. ≥ 3000 identified peptides show the strongest influence of LB on the peptide profile and number of bioactive peptides. Shorter peptides are mostly formed by LB and hydrolyzed by ST.
Eva Beck +6 more
wiley +1 more source
Synthetic Strategies for Activity‐Based Probes to Decode Ubiquitin‐Like Modifiers
ABSTRACT Ubiquitin‐like proteins (Ubls) such as SUMO, NEDD8, ISG15, URM1, UFM1, FAT10, ATG8/ATG12, and FUBI are essential regulators of cellular homeostasis, controlling processes from protein stability and trafficking to immune signaling and autophagy.
Saibal Chanda +5 more
wiley +1 more source
Plasma levels of mannan-binding lectin-associated serine proteases are increased in type 1 diabetes patients with insulin resistance. [PDF]
Kietsiriroje N +5 more
europepmc +1 more source
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An Overview of Serine Proteases
Current Protocols in Protein Science, 2001AbstractThis unit summarizes the families of serine proteases and their mechanism of catalysis. Methods for assays and determining substrate specificity are briefly described. The mode of action of commonly available inhibitors is also included.
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Hydrolysis of polyesters by serine proteases
Biotechnology Letters, 2005The substrate specificity of alpha-chymotrypsin and other serine proteases, trypsin, elastase, proteinase K and subtilisin, towards hydrolysis of various polyesters was examined using poly(L-lactide) (PLA), poly(beta-hydroxybutyrate) (PHB), poly(ethylene succinate) (PES), poly(ethylene adipate) (PEA), poly(butylene succinate) (PBS), poly(butylene ...
Hyun-A, Lim, Takao, Raku, Yutaka, Tokiwa
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Inhibition of serine proteases by steroids
Biochemical Pharmacology, 1982Proteolysis of 14C-labeled globin, as well as the hydrolysis of the specific substrate benzoyl tyrosine ethyl ester, by purified bovine chymotrypsin was found to be inhibited by several steroid hormones. The inhibition of chymotrypsin by the steroids was of a competitive nature, with Ki values of 9.9 x 10(-5) M for triamcinolone (9-fluoro-11 beta, 16 ...
M, Mayer, B, Neufeld, Z, Finci
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Genomic overview of serine proteases
Biochemical and Biophysical Research Communications, 2003Serine proteases (SP) are peptidases with a uniquely activated serine residue in the substrate-binding pocket. They represent about 0.6% of all proteins in the human genome. SP are involved in many vital functions such as digestion, blood clotting, fibrinolysis, fertilization, and complement activation and are related to many diseases including cancer,
George M, Yousef +3 more
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Strategies for the inhibition of serine proteases
Cellular and Molecular Life Sciences, 2001Serine proteases have been shown to play a multifarious role in health and disease. As a result, there has been considerable interest in the design and development of synthetic inhibitors of these enzymes. In view of their diverse roles in biological processing events, one of the great challenges in such endeavours has been the need to produce ...
B, Walker, J F, Lynas
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Serine proteases and cardiac function
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2005The serine proteases of the trypsin superfamily are versatile enzymes involved in a variety of biological processes. In the cardiovascular system, the importance of these enzymes in blood coagulation, platelet activation, fibrinolysis, and thrombosis has been well established.
Qingyu, Wu +2 more
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The novel inhibitors of serine proteases
Amino Acids, 2009Thirty optically active nonprotein alpha-amino acids and peptides based thereon have been screened for their ability to interact with bovine trypsin and proteinase K from Tritirachium album Limber, which belong to the group of serine proteases. Both structure-based drug design approach and determination of enzyme activity have been used to identify low
N, Hovhannisyan +7 more
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